Comparison of collagen fibre architecture between slow-twitch cranial and fast-twitch caudal parts of broiler M. latissimus dorsi

Nakamura, Yasunori; Iwamoto, Hisao; Shoji, Tetsuo; Ono, Yasuki

doi:10.1080/00071660301978

Cited by 10 publications

(11 citation statements)

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“…The first observations using scanning electron microscopy (SEM) on formolized muscle samples were presented by Borg and Caulfield (1980) and Rowe (1981), who demonstrated the presence of collagen fibers in various muscles from different animal species. The existence of these collagen fibers was more recently confirmed by Nishimura et al (1996), Jarvinen et al (2002) and Nakamura et al (2003) using the 2 N NaOH cell-maceration digestion technique, originally introduced by Ohtani et al (1991). Unfortunately, the contaminating presence of endomysium made it impossible to observe perimysium continuity with the tendons by this method, nor was it possible with 5 N NaOH cell maceration (Passerieux et al, 2006).…”

Section: Introductionmentioning

confidence: 79%

“…The strength and stability of these crosslinks are different according to pH and temperature (Jaenicke, 1998;Fathima et al, 2004). Indeed, after 2 N NaOH cell maceration at room temperature, only the endomysium and perimysium remain (Trotter and Purslow, 1992;Nakamura et al, 2003), while cell maceration in 5 N NaOH at temperatures below 20°C eliminates the endomysium, whereas the myofibers and perimysium remain (Passerieux et al, 2006).…”

Section: Naoh Cell-maceration Digestion Technique and Semmentioning

confidence: 97%

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Physical continuity of the perimysium from myofibers to tendons: Involvement in lateral force transmission in skeletal muscle

Passerieux

Rossignol

Letellier

et al. 2007

Journal of Structural Biology

104

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Advances in muscle physiology suggest that the perimysium plays a role in the transmission of lateral contractile forces. This hypothesis is strongly supported by our recent demonstration of the existence of "Perimysial Junctional Plates" in bovine Flexor carpi radialis muscle [Passerieux, E., Rossignol, R., Chopard, A., Carnino, A., Marini, J.F., Letellier, T., Delage, J.P. 2006. Structural organization of the perimysium in bovine skeletal muscle: junctional plates and associated intracellular subdomains. J. Struct. Biol. 154 (2), 206-216] However, the overall organization of the perimysium collagen network, as well as its continuity and heterogeneity, have still not been described in detail throughout the entire muscle. We used an extension of the standard NaOH digestion technique and scanning electron microscopy to analyze perimysium architecture in bovine Flexor carpi radialis muscle. First, we observed that the perimysium is made of a highly ordered network of collagen fibers, binding the myofibers from tendon to tendon. We identified basic collagen cable structures, characterized by a straight portion (3 cm long) in the direction of the myofibers and a curved terminal portion at 60 degrees. These cables reach the myofiber surface at the level of the previously described "Perimysial Junctional Plates". At a higher level of organization, these cables stick together to form the walls of numerous tubes arranged in a overlapping honeycomb pattern around the myofibers. At the ends of these tubes, the straight portions of the collagen cables ramify in large bundles that merge with the tendons. Taken together, these observations identify four levels of organization in the perimysium: (i) Perimysial Junctional Plates that constitute the focal attachment between the perimysium and the myofibers, (ii) collagen plexi attaching adjacent myofibers, (iii) a loose lattice of large interwoven fibers, and (iv) honeycomb tubes connecting two tendons. This spatial arrangement of the perimysium supports the view of a complex pattern of lateral force transmission from myofibers to tendons and adjacent muscles.

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Section: Introductionmentioning

confidence: 79%

Section: Naoh Cell-maceration Digestion Technique and Semmentioning

confidence: 97%

Physical continuity of the perimysium from myofibers to tendons: Involvement in lateral force transmission in skeletal muscle

Passerieux

Rossignol

Letellier

et al. 2007

Journal of Structural Biology

104

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“…01). The endomysial sidewall of cells is very thick in the slow-twitch cranial part compared with the fast-twitch caudal part of a normal broiler's latissimus dorsi muscle (Nakamura et al, 2003a). However, the differ- ence in endomysial thickness between slow-twitch PIF muscle and fast-twitch PT and ITL muscles is very small in both broilers and cocks.…”

Section: Discussionmentioning

confidence: 97%

Developmental states of the collagen content, distribution and architecture in thepectoralis,iliotibialis lateralisandpuboischiofemoralismuscles of male Red Cornish × New Hampshire and normal broilers

Nakamura

Iwamoto

Shiba

et al. 2004

British Poultry Science

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1. Developmental states of the collagen content, distribution and architecture in the pectoralis (PT), iliotibialis lateralis (ITL) and puboischiofemoralis (PIF) muscles of male Red Cornish x New Hampshire (RN, 80 d, body weight 2.9 kg) and normal (3.1 kg) broilers were evaluated. 2. In PT muscle the total amount of collagen was significantly greater in RN broilers (3.33 mg/g) than in normal ones (1.71 mg/g). This higher collagen content in RN broilers was based mainly on the closer mesh sizes of endomysial honeycomb. The collagen structures in the perimysia also differed between broiler types, when more collagen fibres were observed in RN broilers. 3. ITL muscle contained total collagen of 4.10 to 5.00 mg/g. Types I and III collagens were distributed on the perimysia at higher percentages in RN broilers (31.6%, 37.2%) than normal (15.6%, 30.8%), respectively. The thick bands of tough collagen fibres characteristic of ITL muscle perimysium in cockerels had not yet developed in these broilers. 4. Total collagen was 4.63 to 6.29 mg/g in PIF material with fascia. In PIF muscle the perimysial collagen fibres had not yet attained their full growth but consisted of densely packed fibrils. PIF muscle was characterised by the earlier maturing collagen structure. 5. These results show that a perimysial collagen structure in broilers is still in an undeveloped state. It is supposed that tenderness of broiler meat is attributed mainly to characteristics of the collagen distribution, in which the majority of types I and III collagens is distributed on the closer mesh of endomysial honeycomb.

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“…Moreover, the endomysial sheets did not show any difference in collagen structure from fast-twitch muscles such as pectoralis and iliotibialis lateralis (Nakamura et al, 2003a;Oshima et al, 2007a, b;Roy et al, 2006Roy et al, , 2007. Nakamura et al (2003b) observed much thicker endomysial wall in the slow-tonic cranial part than the fast-twitch caudal part of the latissimus dorsi muscle in broilers. The endomysia in the 21-d-old chicks had very thin collagen sheets with many slits but were more developed compared with the endomysia of pectoralis and iliotibialis lateralis muscles in one-week-old chicks (Oshima et al, 2007a, b).…”

Section: Nutrition and Collagen Architecturementioning

confidence: 93%

Collagen content and architecture of thepuboischiofemoralismuscle in male chicks and broilers with different growth rates on various nutritional planes

Das

Roy

Oshima

et al. 2009

British Poultry Science

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1. Various growth rates of chickens were induced with different nutritional regimes, and the collagen content and architecture of the medial part of the puboischiofemoralis muscle were compared among 21-d-old chicks and 80- or 95-d-old broilers. 2. The percentage muscle weight relative to live weight increased from chicks to 80-d-old broilers and the 95-d-old broilers attained the largest percentage. An inter-relationship of the percentage muscle weight and the growth rates of birds could not be determined. 3. Collagen concentration was related to the growth rates for the first 21 d post hatching and maintained the same level during the later stages up to 80 d. The 95-d-old broilers, that were subjected to early rapid growth followed by restricted later growth, had the highest collagen content. 4. On SEM (Scanning Electron Microscopy) photographs, endomysial honeycombs were small and encircled by perimysia of a collagen network with small mesh size. Thin and thick perimysia were distinguished and the expanded portion of thick perimysia was also observed. Generally, the perimysia were made up of rough collagen tissue where fatty tissue developed, especially in the broilers. 5. Perimysial collagen fibres with mainly transverse striation were divided into two fundamental types, wide collagen platelets and narrow cords. With growth from the chick to broiler stage, features of the collagen fibres did not change regardless of expansion of the thick perimysia. Endomysia increased slightly from thin to thick meshwork as growth progressed. However, the collagen architecture of the muscle in broilers did not change under different nutritional regimes. 6. In conclusion, the puboischiofemoralis muscle of chickens develops relative to live weight when later growth is limited in broilers, but the collagen architecture is not affected by the different growth rates.

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Comparison of collagen fibre architecture between slow-twitch cranial and fast-twitch caudal parts of broiler M. latissimus dorsi

Cited by 10 publications

References 0 publications

Physical continuity of the perimysium from myofibers to tendons: Involvement in lateral force transmission in skeletal muscle

Physical continuity of the perimysium from myofibers to tendons: Involvement in lateral force transmission in skeletal muscle

Developmental states of the collagen content, distribution and architecture in thepectoralis,iliotibialis lateralisandpuboischiofemoralismuscles of male Red Cornish × New Hampshire and normal broilers

Collagen content and architecture of thepuboischiofemoralismuscle in male chicks and broilers with different growth rates on various nutritional planes

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